ID U2CCC5_9BACE Unreviewed; 1053 AA.
AC U2CCC5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=HMPREF1981_03052 {ECO:0000313|EMBL:ERI81663.1};
OS Bacteroides pyogenes F0041.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1321819 {ECO:0000313|EMBL:ERI81663.1, ECO:0000313|Proteomes:UP000016496};
RN [1] {ECO:0000313|EMBL:ERI81663.1, ECO:0000313|Proteomes:UP000016496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0041 {ECO:0000313|EMBL:ERI81663.1,
RC ECO:0000313|Proteomes:UP000016496};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERI81663.1}.
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DR EMBL; AWSV01000155; ERI81663.1; -; Genomic_DNA.
DR RefSeq; WP_021646811.1; NZ_KE993153.1.
DR AlphaFoldDB; U2CCC5; -.
DR PATRIC; fig|1321819.3.peg.2820; -.
DR HOGENOM; CLU_002346_0_2_10; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000016496; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1053
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004624284"
FT DOMAIN 759..1036
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1053 AA; 121023 MW; 8040F14DB330A68B CRC64;
MKTPLYTFLS VFLFFTATLS AENVPWQNPQ VNEINREPMH AHFIPFVNES YALKQRSLPA
EVRFDVNSAA ERRISLDGTW QFLYSRNDGL APRDFHKTDY STRGWKRIQV PGSWELQGFD
APIYTDTRYP FPANPPHVPS DYNPVGAYVR EFTVPADWKG LDVFLDFEGV ESAYYVWVNG
ELAGYAEDSR LPSHFNITRL LRKGRNKLAV KVFRYSDGSY LEGQDYWKYS GIERSVYLYA
RPQNRVKDFK MTAGLTNGYK DGDLSLDVFL HRPQAGMEVE VKVLDGGEVI YNRRKAVASE
LDTLMAERHV FPAVKTWNAE TPHTYTLVVN TFDKEGRSLE SFTHLFGFRT VEMRNGMQQI
NGKTVLFKGV NRHEHDPLTG RTITVASMLQ DIRLMKQFNL NAVRNCHYPN NYAWYELCTE
FGLYLIDEAN IESHGMEDHP DGTLANYPDW ELPFIQRMDR MVARDRNVTA VVTWSLGNES
GYGKHFETLY KRTKEADPTR PVQYEGGGYN GKSDIYCPMY ARIWALRKHV NQRDPRPMIL
CEYAHAMGNS VGNLQDYWDL IYKYDQLQGG FIWDWVDQTF LQKDENERPI WAFGGDMGFA
GVVNDSNFCA NGLVAADRSL HPHIWEVKKV LQYVHFEPVA FTSGRIRIVN RHDFTGLERY
MLHWAVECEG RAVQEGKTEF PPIVPQSSGE MELPLQPHPA DGKEYFLTLR VFTKEDAPMI
PKGHEVAIEQ WALPVSPVER KVRPVEGALS VMRSDGTVAL KGDRFLLSFS TRTGEMTELN
YHGKNLIREG LQPNFWRPLT DNDIPNGHLY RCAAWRNAGR ELVLKDMKVT ETPDGKLATV
VVNYRMEQQK SDLRITYQVR PNGAIRVNMH FVPGSIELSE MPRFGMRMIL GAEYEDMSWF
GRGPHETYAD RKSGALIGLY RQSVWEQYHP YVRAQETGNH CDVRWVALRN SAGEGLLVTG
EQPLSVSAWN FPMEDLEYRP SQVERRHGGS IVKKEMVWLN IDHKQMGVGG DNTWGAQVHP
EYTITPHEQT YGFTLQPLSA GEDAADKANL FWF
//
